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Information on EC 6.1.1.17 - glutamate-tRNA ligase and Organism(s) Homo sapiens

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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
glurs, glutaminyl-trna synthetase, glutamyl-trna synthetase, glurs2, trna modifying enzyme, glurs1, glutamyl trna synthetase, discriminating glurs, glursat, glutamyl-transfer ribonucleic acid synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bifunctional aminoacyl-tRNA synthetase
UniProt
bifunctional glutamate/proline-tRNA ligase
UniProt
GluRS
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-
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Glutamate--tRNA ligase
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-
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Glutamate-tRNA synthetase
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-
-
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Glutamic acid translase
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-
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Glutamic acid tRNA ligase
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-
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Glutamyl tRNA synthetase
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-
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glutamyl-prolyl tRNA synthetase
Glutamyl-transfer ribonucleate synthetase
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Glutamyl-transfer ribonucleic acid synthetase
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Glutamyl-transfer RNA synthetase
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Glutamyl-tRNA synthetase
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-
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P85
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-
-
-
additional information
-
cf. EC 6.1.1.15
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aminoacylation
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esterification
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-
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-
SYSTEMATIC NAME
IUBMB Comments
L-glutamate:tRNAGlu ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9068-76-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-glutamate + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
show the reaction diagram
-
mitochondrial glutamyl-tRNA synthetase efficiently aminoacylates both tRNAGln to form Glu-tRNAGln and tRNAGlu to form Glu-tRNAGlu
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-
?
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-glutamate + tRNAGlu
AMP + diphosphate + L-glutamyl-tRNAGlu
show the reaction diagram
additional information
?
-
-
the glutamyl-prolyl tRNA synthetase determines the specificity of the heterotetrameric GAIT complex suppressing translation of selected mRNAs in interferon-gamma-activated monocytic cells by binding to a 3' UTR element in target mRNAs, critical role of EPRS WHEP domains in targeting and regulating GAIT complex binding to RNA, mechanism, overview. The enzyme is essential in regulating inflammatory gene expression
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017
tRNAGln
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-
0.00027
tRNAGlu
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.95
tRNAGln
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-
0.31
tRNAGlu
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
560
tRNAGln
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-
1148
tRNAGlu
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
under conditions of stress, several MSC components, including EPRS, methionyl-tRNA synthetase (MRS), lysyl-tRNA synthetase (KRS), AIMP1 and AIMP2, are released from the complex through post-translational modifications to exert activities during non-translational events such as inflammation, cell metabolism, angiogenesis, and tumorigenesis. Phosphorylation is the critical regulatory mechanism that determines the non-translational function of ARSs in cells, overview
physiological function
the multi-tRNA synthetase complex (MSC) component glutamyl-prolyl-tRNA synthetase (EPRS) switched its function following viral infection and exhibited potent antiviral activity. Infection-specific phosphorylation of EPRS at a Ser induces its dissociation from the MSC, after which it is guided to the antiviral signaling pathway, where it interacts with PCBP2, a negative regulator of mitochondrial antiviral signaling protein (MAVS) that is critical for antiviral immunity. EPRS protects MAVS from PCBP2-mediated ubiquitination. The stimulus-inducible activation of MAVS by enzyme EPRS suggests an unexpected role for the MSC as a regulator of immune responses to viral infection. Phosphorylation of EPRS at a Ser is the driving force that leads to the antiviral roles of EPRS in regulating MAVS
additional information
the enzyme is part of a multi-tRNA synthetase complex (MSC)
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SYEM_HUMAN
523
0
58689
Swiss-Prot
Mitochondrion (Reliability: 2)
SYEP_HUMAN
1512
0
170591
Swiss-Prot
other Location (Reliability: 3)
H6WCP5_HUMAN
863
0
97571
TrEMBL
other Location (Reliability: 3)
V9GYZ6_HUMAN
968
0
109041
TrEMBL
other Location (Reliability: 3)
Q3KQZ8_HUMAN
975
0
109939
TrEMBL
other Location (Reliability: 3)
B4DKX5_HUMAN
988
0
111258
TrEMBL
other Location (Reliability: 3)
Q8NAJ6_HUMAN
717
0
81798
TrEMBL
other Location (Reliability: 5)
H3BTB7_HUMAN
506
0
56825
TrEMBL
Mitochondrion (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
172000
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-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
infection-specific phosphorylation of EPRS at a Ser induces its dissociation from the MSC, after which it is guided to the antiviral signaling pathway, where it interacts with PCBP2, a negative regulator of mitochondrial antiviral signaling protein (MAVS) that is critical for antiviral immunity
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S990A
site-directed mutagenesis, the mutant is unable to rescue virus-infected cells
S990D
site-directed mutagenesis, the mutation markedly inhibits viral replication in cells
additional information
siRNA-mediated enzyme knockout in HEK-293T cells. Cells in which EPRS is knocked down show considerable attenuation of the production of antiviral cytokines (IFN-beta and interleukin-6) following viral infection or treatment with the synthetic double-stranded RNA poly(I:C). Activation of the interferon-related signaling molecules IRF3 and STAT1 is significantly lower in cells in which EPRS is knocked down than in their EPRS-sufficient counterparts
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant tagged wild-type and mutant enzymes from Escherichia coli strain Escherichia coli BL21-CodonPlus (DE3)-RIPL by affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of C-terminally His-tagged, full-length EPRS
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quantitative real-time PCR enzyme expression analysis, recombinant expression of tagged wild-type and mutant enzymes in Escherichia coli strain Escherichia coli BL21-CodonPlus (DE3)-RIPL
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
requirement for sensing by the immune system in the induction of EPRS expression during infection with an RNA virus
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jia, J.; Arif, A.; Ray, P.S.; Fox, P.L.
WHEP domains direct noncanonical function of glutamyl-prolyl tRNA synthetase in translational control of gene expression
Mol. Cell
29
679-690
2008
Homo sapiens
Manually annotated by BRENDA team
Nagao, A.; Suzuki, T.; Katoh, T.; Sakaguchi, Y.; Suzuki, T.
Biogenesis of glutaminyl-mt tRNAGln in human mitochondria
Proc. Natl. Acad. Sci. USA
106
16209-16214
2009
Homo sapiens
Manually annotated by BRENDA team
Lee, E.Y.; Lee, H.C.; Kim, H.K.; Jang, S.Y.; Park, S.J.; Kim, Y.H.; Kim, J.H.; Hwang, J.; Kim, J.H.; Kim, T.H.; Arif, A.; Kim, S.Y.; Choi, Y.K.; Lee, C.; Lee, C.H.; Jung, J.U.; Fox, P.L.; Kim, S.; Lee, J.S.; Kim, M.H.
Infection-specific phosphorylation of glutamyl-prolyl tRNA synthetase induces antiviral immunity
Nat. Immunol.
17
1252-1262
2016
Homo sapiens (P07814), Mus musculus (Q8CGC7), Mus musculus C57BL/6 (Q8CGC7)
Manually annotated by BRENDA team